Luciferase Antibody (Luci 21 1-107) [Alexa Fluor® 750] Summary
Immunogen |
This Luciferase Antibody (Luci 21 1-107) was developed against luciferase protein from Photinus pyralis (North American firefly). [UniProt# P08659]. |
Localization |
Peroxisome |
Specificity |
This Luciferase Antibody (Luci 21 1-107) is specific for Luciferase, recognizing a peptide consisting of the first 258 amino acids. Further epitope mapping has not been done at this time. |
Isotype |
IgG1 Kappa |
Clonality |
Monoclonal |
Host |
Mouse |
Purity |
Protein A or G purified |
Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
Dilutions |
- Flow Cytometry
- Immunocytochemistry/ Immunofluorescence
- Immunohistochemistry
- Immunohistochemistry-Frozen
- Immunohistochemistry-Paraffin
- Western Blot
|
Application Notes |
Optimal dilution of this antibody should be experimentally determined. |
Reactivity Notes
Photinus pyralis (North American firefly).
Packaging, Storage & Formulations
Storage |
Store at 4C in the dark. |
Buffer |
50mM Sodium Borate |
Preservative |
0.05% Sodium Azide |
Purity |
Protein A or G purified |
Notes
Alexa Fluor (R) products are provided under an intellectual property license from Life Technologies Corporation. The purchase of this product conveys to the buyer the non-transferable right to use the purchased product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components, or any materials made using the product or its components, in any activity to generate revenue, which may include, but is not limited to use of the product or its components: (i) in manufacturing; (ii) to provide a service, information, or data in return for payment; (iii) for therapeutic, diagnostic or prophylactic purposes; or (iv) for resale, regardless of whether they are resold for use in research. For information on purchasing a license to this product for purposes other than as described above, contact Life Technologies Corporation, 5791 Van Allen Way, Carlsbad, CA 92008 USA or outlicensing@lifetech.com. This conjugate is made on demand. Actual recovery may vary from the stated volume of this product. The volume will be greater than or equal to the unit size stated on the datasheet.
Alternate Names for Luciferase Antibody (Luci 21 1-107) [Alexa Fluor® 750]
Background
Luciferase is a generic term for a group of oxidative enzymes used in bioluminescence. Firefly (Photinus pyralis) and bacterial luciferase enzymes are commonly used in assay systems such as cell viability assays, reporter gene assays, and for in vivo imaging. Bacterial luciferases are flavoenzymes composed of two subunits each encoded by the luxA and luxB genes, while the firefly luciferase is a single polypeptide specified by the luc gene (1). Firefly luciferase (theoretical molecular weight: 61 kDa) oxidizes the substrate luciferin to oxyluciferin in a bioluminescent reaction requiring Mg2+ and ATP (2,3). This reaction produces a flash of yellow-green light with an emission peak around 560nm that can be detected by a luminometer (3). Firefly luciferase has become one of the more widely used reporter proteins and is an excellent tool for the study of gene expression, given that the amount of light emitted is directly proportional to luciferase activity (4).
The luciferase assay is fast and sensitive, differentiating itself from the CAT (chloramphenicol acetyltransferase) assay because it does not require a radioactive substrate.
References
1. Eun, H. (1996). Marker/Reporter enzymes. Enzymology Primer for Recombinant DNA Technology, 567-645. doi:10.1016/b978-012243740-3/50011-9
2. McNabb, D. S., Reed, R., & Marciniak, R. A. (2005). Dual luciferase assay system for rapid assessment of gene expression in Saccharomyces cerevisiae. Eukaryotic Cell, 4(9), 1539-1549. doi:10.1128/ec.4.9.1539-1549.2005
3. Fraga, H. (2008). Firefly luminescence: A historical perspective and recent developments. Photochemical & Photobiological Sciences, 7(2), 146-158. doi:10.1039/b719181b
4. Younes, A., Lukyanenko, Y. O., Lyashkov, A. E., Lakatta, E. G., & Sollott, S. J. (2011). A bioluminescence method for direct measurement of phosphodiesterase activity. Analytical Biochemistry, 417(1), 36-40. doi:10.1016/j.ab.2011.05.036
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are
guaranteed for 1 year from date of receipt.
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